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4UXX

Structure of delta4-DgkA with AMPPCP in 9.9 MAG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004143molecular_functionATP-dependent diacylglycerol kinase activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006654biological_processphosphatidic acid biosynthetic process
A0008610biological_processlipid biosynthetic process
A0008654biological_processphospholipid biosynthetic process
A0009411biological_processresponse to UV
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004143molecular_functionATP-dependent diacylglycerol kinase activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006654biological_processphosphatidic acid biosynthetic process
B0008610biological_processlipid biosynthetic process
B0008654biological_processphospholipid biosynthetic process
B0009411biological_processresponse to UV
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004143molecular_functionATP-dependent diacylglycerol kinase activity
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006629biological_processlipid metabolic process
C0006654biological_processphosphatidic acid biosynthetic process
C0008610biological_processlipid biosynthetic process
C0008654biological_processphospholipid biosynthetic process
C0009411biological_processresponse to UV
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 1121
ChainResidue
CGLU28
CGLU76
CACP1123

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN C 1122
ChainResidue
CGLU76
CACP1123

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1121
ChainResidue
AASN27
AALA29
AARG32

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP C 1123
ChainResidue
BTYR16
BHOH2001
CGLU28
CASN72
CGLU76
CGLU85
CTYR86
CHIS87
CSER90
CGLY91
CLYS94
CASP95
CZN1121
CZN1122
COLC1125
CHOH2004
BARG9

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 1122
ChainResidue
AARG81
BGLU88
BLEU89
BSER90
BARG92

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1122
ChainResidue
AGLU28
AGLU76
AACT1123

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1123
ChainResidue
AGLU28
AGLU76
ANA1122

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC C 1124
ChainResidue
BARG9
BILE10
CALA30
CGLN33
CGLU34
CCYS113
COLC1125

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OLC B 1123
ChainResidue
ASER17
ACYS113
ATRP117
BGLU34
BALA37
BILE44
BGLU69
BASN72
BLEU102
BOLC1124

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC B 1124
ChainResidue
AILE10
ATRP117
BGLN33
BGLU34
BTRP112
BTRP117
BOLC1123

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC A 1124
ChainResidue
ATRP18
ATRP25
AILE26

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OLC A 1125
ChainResidue
AGLN33
AGLU34
AALA37
AILE44
AVAL62
AALA108
AVAL109
ATRP112
ALEU116
BLEU39
BLEU40
BTRP47

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OLC C 1125
ChainResidue
BALA13
BSER17
CGLU69
CASN72
CSER98
CLEU102
CILE106
CVAL109
CACP1123
COLC1124

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 1125
ChainResidue
BGLU76
BGLY83
BSER84
BGLU85
BTYR86
BHIS87
BLYS94
BNA1126

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 1126
ChainResidue
BGLU28
BGLU76
BACT1125

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA C 1126
ChainResidue
CGLU88
CGLU88

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 1126
ChainResidue
AHIS119

Functional Information from PROSITE/UniProt
site_idPS01069
Number of Residues12
DetailsDAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
ChainResidueDetails
AGLU69-ASP80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues87
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:8071224
ChainResidueDetails
AALA1-ALA30
BALA1-ALA30
CALA1-ALA30

site_idSWS_FT_FI2
Number of Residues99
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
ChainResidueDetails
APHE31-TRP47
AASP51-VAL68
BPHE31-TRP47
BASP51-VAL68
CPHE31-TRP47
CASP51-VAL68

site_idSWS_FT_FI3
Number of Residues6
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
ChainResidueDetails
ALEU48-VAL50
BLEU48-VAL50
CLEU48-VAL50

site_idSWS_FT_FI4
Number of Residues75
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:8071224
ChainResidueDetails
AGLU69-LYS94
BGLU69-LYS94
CGLU69-LYS94

site_idSWS_FT_FI5
Number of Residues69
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:8071224
ChainResidueDetails
AASP95-SER118
BASP95-SER118
CASP95-SER118

site_idSWS_FT_FI6
Number of Residues6
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
ChainResidueDetails
AHIS119-GLY121
BHIS119-GLY121
CHIS119-GLY121

site_idSWS_FT_FI7
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26673816
ChainResidueDetails
AGLU69
BGLU69
CGLU69

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
ChainResidueDetails
AARG9
BARG9
CARG9

site_idSWS_FT_FI9
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
AALA13
BALA13
CALA13

site_idSWS_FT_FI10
Number of Residues15
DetailsBINDING: BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
ChainResidueDetails
ATYR16
BLYS94
CTYR16
CGLU28
CGLU76
CGLU85
CLYS94
AGLU28
AGLU76
AGLU85
ALYS94
BTYR16
BGLU28
BGLU76
BGLU85

site_idSWS_FT_FI11
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
ChainResidueDetails
AARG22
BARG22
CARG22

site_idSWS_FT_FI12
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
AALA30
BALA30
CALA30

site_idSWS_FT_FI13
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
ChainResidueDetails
ATRP47
BTRP47
CTRP47

site_idSWS_FT_FI14
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
ChainResidueDetails
AARG55
BARG55
CARG55

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
ChainResidueDetails
AGLU69
BGLU69
CGLU69

site_idSWS_FT_FI16
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
ASER98
BSER98
CSER98

site_idSWS_FT_FI17
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
ChainResidueDetails
ATRP112
BTRP112
CTRP112

217705

PDB entries from 2024-03-27

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